Riboflavin kinase
     (EC 2.7.1.26)
     (Flavokinase)
FMN adenylyltransferase
     (EC 2.7.7.2)
     (FAD pyrophosphorylase)
     (FAD synthetase)

Gene name

Name:

ribF

From

Pseudomonas fluorescens

[TaxID: 294]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 49323 / NCIMB 10586; PubMed=2121716 [NCBI, ExPASy, EBI, Israel, Japan] Isaki L., Beers R., Wu H.C.; "Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II gene (lsp) and flanking genes."; J. Bacteriol. 172:6512-6517(1990).

Comments

CATALYTIC ACTIVITY: ATP + riboflavin = ADP + FMN.
CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD.
PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1 .
PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin: step 1/1 .
SIMILARITY: Belongs to the ribF family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M35367; AAA26021.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E37152; E37152.

3D structure databases

HSSP

Q969G6; 1NB9. [HSSP ENTRY / PDB]

ModBase

P22990.

Ontologies

GO:0003919;	Molecular function: FMN adenylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008531;	Molecular function: riboflavin kinase activity (inferred from electronic annotation from InterPro).
GO:0009231;	Biological process: riboflavin biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR015864; FAD_synthase.
IPR015865; Riboflavin_kinase.
IPR002606; Riboflavin_kinase/FAD_synth.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.30.30; Riboflavin_kinase; 1.
G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.

PANTHER

PTHR22749; Riboflavin_kinase; 1.

Pfam

PF06574; FAD_syn; 1.
PF01687; Flavokinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF004491; FAD_Synth; 1.

ProDom

PD003662; FAD_Synth; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR00083; ribF; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

FAD; FMN; Multifunctional enzyme; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 311`	`311`		`Riboflavin biosynthesis protein ribF.`	`PRO_0000194141`

Sequence information

Length: 311 AA [This is the length of the unprocessed precursor]

Molecular weight: 33898 Da [This is the MW of the unprocessed precursor]

CRC64: E4ED0EF97C064D60 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQLVRGLHNL RPEHRGCVAT IGNFDGVHRG HQAILARLRE RAVELGVPSC VVIFEPQPRE 

        70         80         90        100        110        120 
FFTPETAPAR LALARQAATA GGEGVDRVLC LAFNQRLRSL SAAEFVDRIL VDGLGVQHLE 

       130        140        150        160        170        180 
VGDDFHFGCD RVGDFDFLQH AGVNQGFTVE AAQTVELDGL RVSSTQVRNA LAAADFDLAE 

       190        200        210        220        230        240 
RLLGRPFRIA GRVLHGQKLA RQLGTPTANV QLKRRRVPLT GVYLVSVDID GQSWPGVANI 

       250        260        270        280        290        300 
GVRPTVAGDG KAHLEVHLLD FAGDLYDRRL TVVFHQKLRE EQRFASLEAL KTAINADVAA 

       310 
ARALAAPSAH R

P22990 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools